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CDPAS_STAMF
ID   CDPAS_STAMF             Reviewed;         176 AA.
AC   A3DM64;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=CDP-archaeol synthase {ECO:0000255|HAMAP-Rule:MF_01117};
DE            EC=2.7.7.67 {ECO:0000255|HAMAP-Rule:MF_01117};
DE   AltName: Full=CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase {ECO:0000255|HAMAP-Rule:MF_01117};
GN   Name=carS {ECO:0000255|HAMAP-Rule:MF_01117}; OrderedLocusNames=Smar_0617;
OS   Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Staphylothermus.
OX   NCBI_TaxID=399550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA   Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA   Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA   Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA   Woese C., Bristow J., Kyrpides N.;
RT   "The complete genome sequence of Staphylothermus marinus reveals
RT   differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL   BMC Genomics 10:145-145(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=21304655; DOI=10.4056/sigs.30527;
RA   Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT   type strain F1.";
RL   Stand. Genomic Sci. 1:183-188(2009).
CC   -!- FUNCTION: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-
CC       glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-
CC       phosphate (DGGGP) and CTP. This reaction is the third ether-bond-
CC       formation step in the biosynthesis of archaeal membrane lipids.
CC       {ECO:0000255|HAMAP-Rule:MF_01117}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + CTP +
CC         H(+) = CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol + diphosphate;
CC         Xref=Rhea:RHEA:25690, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:58837, ChEBI:CHEBI:58838; EC=2.7.7.67;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01117};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01117};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01117}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01117};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01117}.
CC   -!- SIMILARITY: Belongs to the CDP-archaeol synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01117}.
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DR   EMBL; CP000575; ABN69724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3DM64; -.
DR   SMR; A3DM64; -.
DR   STRING; 399550.Smar_0617; -.
DR   EnsemblBacteria; ABN69724; ABN69724; Smar_0617.
DR   KEGG; smr:Smar_0617; -.
DR   eggNOG; arCOG04106; Archaea.
DR   HOGENOM; CLU_105710_0_0_2; -.
DR   OMA; GKTWRGT; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000254; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043338; F:CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01117; CDP_archaeol_synth; 1.
DR   InterPro; IPR032690; CarS.
DR   InterPro; IPR002726; CarS_archaea.
DR   PANTHER; PTHR39650; PTHR39650; 1.
DR   Pfam; PF01864; CarS-like; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..176
FT                   /note="CDP-archaeol synthase"
FT                   /id="PRO_0000298288"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01117"
SQ   SEQUENCE   176 AA;  20205 MW;  D0BACD5B7BD33FFD CRC64;
     MSGYMISPEY YFIYWFLKYY LSPMIANASP VLVKGIHRID FSHIFIDGKP LFGKNKTWEG
     FYVGVLMGFL TSIGIGIILC EEEYILIGLG SSIFALIGDL LGSFIKRRMN IASGEPLPII
     DQLDFALMAT LYYYFLGIEE FISYPLYILY SLIIILALHI ITNNIAYYLG VKDKRW
 
 
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